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The orthologous group consisting of BAPKO_0422, BB0405 and BG0407 are proposed to play a role in virulence by binding to host fH, therefore abrogating the host complement response and reducing antigenicity of surface exposed loops.
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Hemagglutinin plays a major role in determining host specificity since it is responsible for viral binding to host cell receptors and penetration of host membranes [5], [6], [7].
There are some examples of PfEMP1 variants where binding to host receptors is localized to a single domain (for example, CIDRα binding CD36 [49] or DBLβC2 binding ICAM-1 [50].
Pathogens such as Candida albicans, Neisseria meningiditis, and Streptococcus pneumonia have been shown to bind host FH, and that FH binding in N. gonorrhea and B. burgdorferi provides protection against complement killing in vitro [25] [29].
Alternatively, binding to certain FH family proteins may not be essential to the spirochetes, as previous studies indicate that B. burgdorferi are able to infect and cause disease in FH-deficient mice [57].
ALBI assays were performed to detect specific binding to human fH.
F. tularensis employs bacterial surface proteins to colonize the host cells by binding to specific host-cell receptors.
Much rather, it was required for efficient movement and binding to the host cell.
FimH mediates binding to mannose containing host receptors.
(E) PBZ treatment does not affect the binding of HCV to host cells.
(F) The down-regulation of 5-HT2AR does not attenuate the binding of HCV to host cells.
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